1. According to the Michaelis-Menten equation, when is the reaction velocity at half the maximal value (vo = 0.5 Vmax) A. when [S] = 0.5 Km B. when [S] = 1.0 Km C. when vo = kcat [E] D. when vo = kcat / Km 2. The value of Vmax depends on ... A. k1 and k-1 B. k1 and k2 C. k1 only D. k2 only 3. When is Km approximately equal to Kd? A. when k1 is much...
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using the M-M equation that when [S] <<<Km, vo =[S][Et]kcat/Km. 2. What is Vmax? Provide both a mathematical and written description of Vmax? How can Vmax be experimentally altered? How can we use Vmax to determine the turnover number (kcat) of an enzyme-catalyzed reaction? What is the major challenge of determining Vmax from an Michaelis-Menten plot?
D-Lactose is the substrate for B-galactosidase. Given Vo = kcat [Et] [S]/km + [S], calculate [S], when Km = 4.0 nM, V. = 10.5 M s', kcat = 500 s, and [Et] = 40 uM Calculate the catalytic efficiency. Below is a double-reciprocal plot for an enzyme reaction in the absence and presence of of inhibitor. Give the equation for the line. Calculate Vmax and Km for the enzyme and enzyme plus inhibitor. Which type of inhibition is apparent. 0.10...
Kcat =30.0 s-1
Km= 0.005 M
Operating at 1/4 Vmax
What is [S] ?
The solutions manuel doesn't explain the problem well. Whete
does the 0.33 km come from?
For part 2 : Plug in [S]= 1/2 Km, 2 Km, and 10 Km
Where does the 1.5 Km come from?
Answer (a) Here we want to find the value of [S] when Vo = 0.25 V max. The Michaelis-Menten equation is V = Vmax[S]/(Km + [SD so V = Vmax...
3) For the simplified representation of an enzyme-catalyzed
reaction shown below, the statement “ES is in steady-state” means
that:
A) k2 is very slow.
B) k1= k2.
C) k1= k-1.
D) k1[E][S] = k-1[ES] + k2[ES].
E) k1[E][S] = k-1[ES].
3) For the simplified representation of an enzyme-catalyzed reaction shown below, the statement “ES is in steady-state" means that: k, k, E+S <> ES Z E +P - k1 A) k2 is very slow. B) Kı= k2. C) K1= k-1....
For enzymes in which the slowest (rate-limiting) step is the reaction: K2 ES → E+P Km becomes equivalent to: A) kcat. B) the [S] where V0 = Vmax. C) the dissociation constant, Kd, for the ES complex. D) the maximal velocity. E) the turnover number. The answer is C), could you please explain?
30. Describe the difference between transition state and intermediate using energy diagrams. 31. For enzymes in which the slowest (rate-limiting) step is the reaction k2 ES P Km becomes equivalent to: A. Kcat- B. the [S], where Vo Vmax C. the dissociation constant, Ka, for the ES complex. D. the maximal velocity. E. the turnover number. 33. Draw a schematic for sequential mechanism 32. An enzyme "ABase" catalyzes the following reaction: A B. You found that for [E] 4 nM,...
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit of . The value of Vmax for. the same reaction is with the unit of . Be sure to give the values with the correct number of significant figures. You might have to construct a kinetic plot. For units, choose one answer from (uM, 1/ UM, HM/second, uM x second, mM, 1/mM, second, 1/second, mM/second, mM x second) vo (mM/sec) Glucose concentration (mm) 0.10...
michaelis menten and kinetics help
2. A few years after Michaelis Menten published their work Briggs and Haldane came along and expanded it using the steady state assumption. i) Based on kinetic scheme 2 how many different ways can ES be produced? i) Using the rate constants in kinetic Scheme 2 at what rate is the ES complex being produced? sed eci iv) Using the rate constants in kinetic Scheme 2 at what rate is the ES complex being destroyed?...
What is substrate concentration, expressed as a multiple of Km, when an enzyme reaction is observed to have an initial rate Vo = 0.75 Vmax. Select one: O a. [S] = 0.33 x km O b. [S] = 0.25 km O c. [S] = 0.75 x Km O d. [S] = 0.3 x km O e. [S] = 0.5 x km Check Next page ime Jump to...